STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CAZ94614.1ATPase belonging to the MoxR-like family. In Paracoccus denitrificans, MoxR is involved in the regulation of formation of active methanol dehydrogenase. MoxR-like ATPases have been proposed to function with VWA domain proteins to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Specificity unclear. (332 aa)    
Predicted Functional Partners:
CAZ94615.1
vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules. Contains two N-terminal transmembrane helices; Localized in the cytoplasmic membrane; Function unclear.
  
 0.922
CAZ94610.1
Conserved integral membrane protein belonging to the DUF95 family. Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
 
    0.853
CAZ94612.1
Conserved hypothetical membrane protein; Contains one central transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
 
    0.837
CAZ94613.1
Conserved hypothetical membrane protein; Contains two transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
 
    0.828
CAZ94611.1
Conserved hypothetical membrane protein; Contains five transmembrane helices; Localized in the cytoplasmic membrane; Conserved hypothetical protein.
  
    0.792
CAZ95552.1
vWA domain protein; Conserved protein belonging to the von Willebrand factor type A (vWA) domain family. Some VWA domain proteins have been proposed to function with MoxR-like ATPases to form a chaperone system involved in the activation of proteins by primarily mediating the insertion of metal cofactors into the substrate molecules; Localized in the cytoplasm; Family membership.
  
 0.719
CAZ94609.1
This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. Contains three transmembrane helices. The arginine occurs at the N terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this protein is unknown; Localized in the cytoplasmic membrane; Family membership.
 
    0.713
CAZ94616.1
Putative protein.
       0.556
CAZ94617.1
Hypothetical protein. Putatively localized in the cytoplasm.
       0.556
CAZ96337.1
Conserved hypothetical protein. Localized in the cytoplasm.
 
  
 0.474
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.